Discovered a versatile mode of protein-complex cooperation key to the establishment of cell polarity
aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity.
Josana Rodriguez, Florent Peglion, Jack Martin, Lars Hubatsch, Jacob Reich, Nisha Hirani, Alicia G Gubieda, Jon Roffey, Artur Ribeiro Fernandes, Daniel St Johnston, Julie Ahringer, and Nathan W Goehring.
Dev Cell, 2017 pp. 1-35.
The conserved polarity effector proteins PAR-3, PAR-6, CDC-42, and atypical protein kinase C (aPKC) form a core unit of the PAR protein network, which plays a central role in polarizing a broad range of animal cell types. To functionally polarize cells, these proteins must activate aPKC within a spatially defined membrane domain on one side of the cell in response to symmetry-breaking cues. Using the Caenorhabditis elegans zygote as a model, we find that the localization and activation of aPKC involve distinct, specialized aPKC-containing assemblies: a PAR-3-dependent assembly that responds to polarity cues and promotes efficient segregation of aPKC toward the anterior but holds aPKC in an inactive state, and a CDC-42-dependent assembly in which aPKC is active but poorly segregated. Cycling of aPKC between these distinct functional assemblies, which appears to depend on aPKC activity, effectively links cue-sensing and effector roles within the PAR network to ensure robust establishment of polarity.